UbcH6 interacts with and ubiquitinates the SCA1 gene product ataxin-1

Sunghoi Hong, Soyeon Lee, Ssang Goo Cho, Seong Man Kang

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

UbcH6 is a member of an evolutionally conserved subfamily of E2 ubiquitin-conjugating enzymes. In this study, we report that UbcH6 interacts with and ubiquitinates ataxin-1, the spinocerebellar ataxia type 1 gene product. UbcH6 was identified as an ataxin-1-interacting protein using a yeast two-hybrid screen. UbcH6 co-immunoprecipitates and co-localizes with the ataxin-1 protein in the nucleus. Our binding assays showed that ataxin-1 interacts with UbcH6 through its AXH domain. Interestingly, UbcH6 could ubiquitinate ataxin-1 in the absence of an E3 ligase. The expression level of UbcH6 regulated the rate of ataxin-1 degradation. This study demonstrates that UbcH6 and ataxin-1 are E2-substrate cognate pairs in the ubiquitin-proteasome system.

Original languageEnglish
Pages (from-to)256-260
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume371
Issue number2
DOIs
Publication statusPublished - 2008 Jun 27

Fingerprint

Spinocerebellar Ataxias
Genes
Ubiquitin-Conjugating Enzymes
Ubiquitin-Protein Ligases
Proteasome Endopeptidase Complex
Ubiquitin
Ataxin-1
Yeast
Assays
Yeasts
Degradation
Substrates

Keywords

  • Ataxin-1
  • AXH domain
  • UbcH6
  • Ubiquitination

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

UbcH6 interacts with and ubiquitinates the SCA1 gene product ataxin-1. / Hong, Sunghoi; Lee, Soyeon; Cho, Ssang Goo; Kang, Seong Man.

In: Biochemical and Biophysical Research Communications, Vol. 371, No. 2, 27.06.2008, p. 256-260.

Research output: Contribution to journalArticle

@article{cf3f099454a34ce9895fdbd047de810e,
title = "UbcH6 interacts with and ubiquitinates the SCA1 gene product ataxin-1",
abstract = "UbcH6 is a member of an evolutionally conserved subfamily of E2 ubiquitin-conjugating enzymes. In this study, we report that UbcH6 interacts with and ubiquitinates ataxin-1, the spinocerebellar ataxia type 1 gene product. UbcH6 was identified as an ataxin-1-interacting protein using a yeast two-hybrid screen. UbcH6 co-immunoprecipitates and co-localizes with the ataxin-1 protein in the nucleus. Our binding assays showed that ataxin-1 interacts with UbcH6 through its AXH domain. Interestingly, UbcH6 could ubiquitinate ataxin-1 in the absence of an E3 ligase. The expression level of UbcH6 regulated the rate of ataxin-1 degradation. This study demonstrates that UbcH6 and ataxin-1 are E2-substrate cognate pairs in the ubiquitin-proteasome system.",
keywords = "Ataxin-1, AXH domain, UbcH6, Ubiquitination",
author = "Sunghoi Hong and Soyeon Lee and Cho, {Ssang Goo} and Kang, {Seong Man}",
year = "2008",
month = "6",
day = "27",
doi = "10.1016/j.bbrc.2008.04.066",
language = "English",
volume = "371",
pages = "256--260",
journal = "The BMJ",
issn = "0730-6512",
publisher = "Kluwer Academic Publishers",
number = "2",

}

TY - JOUR

T1 - UbcH6 interacts with and ubiquitinates the SCA1 gene product ataxin-1

AU - Hong, Sunghoi

AU - Lee, Soyeon

AU - Cho, Ssang Goo

AU - Kang, Seong Man

PY - 2008/6/27

Y1 - 2008/6/27

N2 - UbcH6 is a member of an evolutionally conserved subfamily of E2 ubiquitin-conjugating enzymes. In this study, we report that UbcH6 interacts with and ubiquitinates ataxin-1, the spinocerebellar ataxia type 1 gene product. UbcH6 was identified as an ataxin-1-interacting protein using a yeast two-hybrid screen. UbcH6 co-immunoprecipitates and co-localizes with the ataxin-1 protein in the nucleus. Our binding assays showed that ataxin-1 interacts with UbcH6 through its AXH domain. Interestingly, UbcH6 could ubiquitinate ataxin-1 in the absence of an E3 ligase. The expression level of UbcH6 regulated the rate of ataxin-1 degradation. This study demonstrates that UbcH6 and ataxin-1 are E2-substrate cognate pairs in the ubiquitin-proteasome system.

AB - UbcH6 is a member of an evolutionally conserved subfamily of E2 ubiquitin-conjugating enzymes. In this study, we report that UbcH6 interacts with and ubiquitinates ataxin-1, the spinocerebellar ataxia type 1 gene product. UbcH6 was identified as an ataxin-1-interacting protein using a yeast two-hybrid screen. UbcH6 co-immunoprecipitates and co-localizes with the ataxin-1 protein in the nucleus. Our binding assays showed that ataxin-1 interacts with UbcH6 through its AXH domain. Interestingly, UbcH6 could ubiquitinate ataxin-1 in the absence of an E3 ligase. The expression level of UbcH6 regulated the rate of ataxin-1 degradation. This study demonstrates that UbcH6 and ataxin-1 are E2-substrate cognate pairs in the ubiquitin-proteasome system.

KW - Ataxin-1

KW - AXH domain

KW - UbcH6

KW - Ubiquitination

UR - http://www.scopus.com/inward/record.url?scp=43149123766&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=43149123766&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2008.04.066

DO - 10.1016/j.bbrc.2008.04.066

M3 - Article

VL - 371

SP - 256

EP - 260

JO - The BMJ

JF - The BMJ

SN - 0730-6512

IS - 2

ER -